Screen for DNA‐damage‐responsive histone modifications identifies H3K9Ac and H3K56Ac in human cells
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Recognition and repair of damaged DNA occurs within the context of chromatin. The key protein components of chromatin are histones, whose post-translational modifications control diverse chromatin functions. Here, we report our findings from a large-scale screen for DNA-damage-responsive histone modifications in human cells. We have identified specific phosphorylations and acetylations on histone H3 that decrease in response to DNA damage. Significantly, we find that DNA-damage-induced changes in H3S10p, H3S28p and H3.3S31p are a consequence of cell-cycle re-positioning rather than DNA damage per se. In contrast, H3K9Ac and H3K56Ac, a mark previously uncharacterized in human cells, are rapidly and reversibly reduced in response to DNA damage. Finally, we show that the histone acetyl-transferase GCN5/KAT2A acetylates H3K56 in vitro and in vivo. Collectively, our data indicate that though most histone modifications do not change appreciably after genotoxic stress, H3K9Ac and H3K56Ac are reduced in response to DNA damage in human cells.
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H3K56 acetylation is negatively regulated by DNA damage in human cells.
“we recently found that H3K9 and H3K56 acetylations (H3K9Ac and H3K56Ac) are negatively regulated by DNA damage20.”
From Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining (2010) · cites this paper as [20]
The observed decrease in H3K56Ac levels was not due to effects of DNA damage on cell-cycle distributions, as this histone mark is not cell cycle regulated.
“the observed decrease in H3K56Ac levels were not due to effects of DNA damage on cell-cycle distributions, as this histone mark is not cell cycle regulated20,35”
From Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining (2010) · cites this paper as [20]
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- Authors
- Tjeertes, J. V., Miller, K. M., & Jackson, S. P.
- Affiliations
- University of Cambridge (GB)
- Corresponding author
- Miller, Kyle M
- Jackson, Stephen P
- Venue
- The EMBO Journal
- Published
- 2009-04-30
- Volume
- 28
- Issue
- 13
- Pages
- 1878-1889
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC2684025
- OpenAlex
- W2046691617
- Cited by
- 347
- References
- 68
- Citations by year
- 2026: 7 · 2025: 10 · 2024: 21 · 2023: 15 · 2022: 16 · 2021: 18 · 2020: 14 · 2019: 17 · 2018: 13 · 2017: 21 · 2016: 21 · 2015: 22 · 2014: 20 · 2013: 31 · 2012: 31
- FWCI
- 13.54
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust (086861/Z/08/Z, 086861)
- Cancer Research UK (A5290)
- Directorate for Biological Sciences
- Biotechnology and Biological Sciences Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- DNA damage response, histone modifications, H3K9 acetylation, H3K56 acetylation, histone acetylation, histone phosphorylation, histone acetyltransferase, chromatin, genotoxic stress
- MeSH terms
- p300-CBP-Associated Factor, Acetylation, Cell Cycle, DNA Damage, DNA Repair, HeLa Cells, Histones, Humans, Phosphorylation, Protein Processing, Post-Translational, Histone Code, Cell Line, Tumor, Histone Acetyltransferases
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